Novel anti-inflammatory peptides from the region of highest similarity between uteroglobin and lipocortin I

L. Miele, E. Cordella-Miele, A. Facchiano, A. B. Mukherjee

Research output: Contribution to journalArticlepeer-review

Abstract

Significant future developments in the effective treatment of inflammatory diseases may arise from non-toxic dual inhibitors of both cyclooxygenase and lipoxygenase pathways in the arachidonate cascade. Inhibition of phospholipase A 2 (PLA 2) (EC 3.1.1.4), may provide such a dual action and recent research has concentrated on the role of PLA 2-inhibitory proteins as possible anti-inflammatory agents. Blastokinin or uteroglobin is a steroid-induced rabbit secretory protein with PLA 2-inhibitory activity. Its biochemical and biological properties have been extensively studied and its crystallographic structure has been resolved at 1.34 Å. Lipocortins are a family of related proteins, which, it has been suggested, mediate the antiinflammatory effects of glucocorticoids. Some proteins of this group have been purified and the complementary DNA sequences of two human lipocortins are known. Lipocortins inhibit PLA 2 in vitro, although their mechanism of action is still unclear. Recombinant lipocortin I inhibits eicosanoid synthesis in isolated perfused lungs from the guinea pig. Here, we report that synthetic oligopeptides corresponding to a region of high amino-acid sequence similarity between uteroglobin and lipocortin I have potent PLA 2 inhibitory activity in vitro and striking anti-inflammatory effects in vivo.

Original languageEnglish
Pages (from-to)726-730
Number of pages5
JournalNature
Volume335
Issue number6192
Publication statusPublished - 1988

ASJC Scopus subject areas

  • General

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